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Trends Endocrinol Metab. 2011 Nov;22(11):429-36. doi: 10.1016/j.tem.2011.07.005. Epub 2011 Aug 24.

The capture of phosphoproteins by 14-3-3 proteins mediates actions of insulin.

Author information

1
MRC Protein Phosphorylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.

Abstract

How does signalling via PI3K-PKB (AKT)-mTORC1-p70S6K and ERK-p90RSK mediate wide-ranging physiological responses to insulin? Quantitative proteomics and biochemical experiments are revealing that these signalling pathways induce the phosphorylation of large and overlapping sets of proteins, which are then captured by phosphoprotein-binding proteins named 14-3-3s. The 14-3-3s are dimers that dock onto dual-phosphorylated sites in a configuration with special signalling and mechanical properties. They interact with the Rab GTPase-activating proteins AS160 and TBC1D1 to regulate glucose uptake into target tissues in response to insulin and energy stress. Dynamic patterns in the 14-3-3-binding phosphoproteome are providing new insights into how insulin triggers coherent shifts in metabolism that are integrated with other cellular response systems.

PMID:
21871813
DOI:
10.1016/j.tem.2011.07.005
[Indexed for MEDLINE]
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